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The N-terminal domain of SV40 large T antigen represses the HER2/neu-mediated transformation and metastatic potential in breast cancers
HER2/neu is known to be overexpressed in approximately 40% of human breast and ovarian cancers and it is associated with increased metastasis and poor prognosis. We have shown previously that the N-terminal domain of simian virus 40 large T antigen (LT425) can act as a transforming suppressor of the...
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| Published in: | FEBS letters 2002-01, Vol.511 (1), p.46-50 |
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| Main Authors: | , , , , |
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| cites | cdi_FETCH-LOGICAL-c426X-3bdf1d87fe64d964da88ab39ac5e193fde433446c95e3c172ace7089957396fb3 |
| container_end_page | 50 |
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| container_start_page | 46 |
| container_title | FEBS letters |
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| creator | Chuang, Tzu-Chao Yu, Yuh-Hua Lin, Yen-Shing Wang, Shan-Shue Kao, Ming-Ching |
| description | HER2/neu is known to be overexpressed in approximately 40% of human breast and ovarian cancers and it is associated with increased metastasis and poor prognosis. We have shown previously that the N-terminal domain of simian virus 40 large T antigen (LT425) can act as a transforming suppressor of the
HER2/
neu oncogene in human ovarian cancer. In the present study, we demonstrate that LT425 can also repress the transforming properties of HER2/neu-overexpressing human breast cancer cells. In addition, the results of a chemotaxis assay and an in vitro chemoinvasion assay further suggest that LT425 can also suppress the metastatic potential of the HER2/neu-transformed breast cancer cells. Taken together, these data clearly suggest that the inhibition of the expression of p185
HER2/neu tyrosine kinase by LT425 is capable of suppressing the HER2/neu-mediated transformation and metastatic potential in breast cancers. |
| doi_str_mv | 10.1016/S0014-5793(01)03277-X |
| format | article |
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HER2/
neu oncogene in human ovarian cancer. In the present study, we demonstrate that LT425 can also repress the transforming properties of HER2/neu-overexpressing human breast cancer cells. In addition, the results of a chemotaxis assay and an in vitro chemoinvasion assay further suggest that LT425 can also suppress the metastatic potential of the HER2/neu-transformed breast cancer cells. Taken together, these data clearly suggest that the inhibition of the expression of p185
HER2/neu tyrosine kinase by LT425 is capable of suppressing the HER2/neu-mediated transformation and metastatic potential in breast cancers.</description><identifier>ISSN: 0014-5793</identifier><identifier>EISSN: 1873-3468</identifier><identifier>DOI: 10.1016/S0014-5793(01)03277-X</identifier><identifier>PMID: 11821047</identifier><language>eng</language><publisher>England: Elsevier B.V</publisher><subject>Antigens, Polyomavirus Transforming - chemistry ; Antigens, Polyomavirus Transforming - genetics ; Antigens, Polyomavirus Transforming - metabolism ; Blotting, Western ; Breast Neoplasms - genetics ; Breast Neoplasms - metabolism ; Breast Neoplasms - pathology ; Cell Division ; Cell Transformation, Neoplastic - genetics ; Cell Transformation, Neoplastic - metabolism ; Cell Transformation, Neoplastic - pathology ; Chemotaxis ; Down-Regulation ; Female ; Gene Expression Regulation, Neoplastic ; Genes, erbB-2 - genetics ; HER2/neu ; Humans ; Metastasis ; Neoplasm Metastasis - genetics ; Neoplasm Metastasis - pathology ; p185 ; Protein Structure, Tertiary ; Receptor, ErbB-2 - antagonists & inhibitors ; Receptor, ErbB-2 - genetics ; Receptor, ErbB-2 - metabolism ; Simian virus 40 large T antigen ; Tumor Cells, Cultured</subject><ispartof>FEBS letters, 2002-01, Vol.511 (1), p.46-50</ispartof><rights>2002 Federation of European Biochemical Societies</rights><rights>FEBS Letters 511 (2002) 1873-3468 © 2015 Federation of European Biochemical Societies</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c426X-3bdf1d87fe64d964da88ab39ac5e193fde433446c95e3c172ace7089957396fb3</citedby><cites>FETCH-LOGICAL-c426X-3bdf1d87fe64d964da88ab39ac5e193fde433446c95e3c172ace7089957396fb3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S001457930103277X$$EHTML$$P50$$Gelsevier$$Hfree_for_read</linktohtml><link.rule.ids>314,780,784,3549,27924,27925,45780</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/11821047$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Chuang, Tzu-Chao</creatorcontrib><creatorcontrib>Yu, Yuh-Hua</creatorcontrib><creatorcontrib>Lin, Yen-Shing</creatorcontrib><creatorcontrib>Wang, Shan-Shue</creatorcontrib><creatorcontrib>Kao, Ming-Ching</creatorcontrib><title>The N-terminal domain of SV40 large T antigen represses the HER2/neu-mediated transformation and metastatic potential in breast cancers</title><title>FEBS letters</title><addtitle>FEBS Lett</addtitle><description>HER2/neu is known to be overexpressed in approximately 40% of human breast and ovarian cancers and it is associated with increased metastasis and poor prognosis. We have shown previously that the N-terminal domain of simian virus 40 large T antigen (LT425) can act as a transforming suppressor of the
HER2/
neu oncogene in human ovarian cancer. In the present study, we demonstrate that LT425 can also repress the transforming properties of HER2/neu-overexpressing human breast cancer cells. In addition, the results of a chemotaxis assay and an in vitro chemoinvasion assay further suggest that LT425 can also suppress the metastatic potential of the HER2/neu-transformed breast cancer cells. Taken together, these data clearly suggest that the inhibition of the expression of p185
HER2/neu tyrosine kinase by LT425 is capable of suppressing the HER2/neu-mediated transformation and metastatic potential in breast cancers.</description><subject>Antigens, Polyomavirus Transforming - chemistry</subject><subject>Antigens, Polyomavirus Transforming - genetics</subject><subject>Antigens, Polyomavirus Transforming - metabolism</subject><subject>Blotting, Western</subject><subject>Breast Neoplasms - genetics</subject><subject>Breast Neoplasms - metabolism</subject><subject>Breast Neoplasms - pathology</subject><subject>Cell Division</subject><subject>Cell Transformation, Neoplastic - genetics</subject><subject>Cell Transformation, Neoplastic - metabolism</subject><subject>Cell Transformation, Neoplastic - pathology</subject><subject>Chemotaxis</subject><subject>Down-Regulation</subject><subject>Female</subject><subject>Gene Expression Regulation, Neoplastic</subject><subject>Genes, erbB-2 - genetics</subject><subject>HER2/neu</subject><subject>Humans</subject><subject>Metastasis</subject><subject>Neoplasm Metastasis - genetics</subject><subject>Neoplasm Metastasis - pathology</subject><subject>p185</subject><subject>Protein Structure, Tertiary</subject><subject>Receptor, ErbB-2 - antagonists & inhibitors</subject><subject>Receptor, ErbB-2 - genetics</subject><subject>Receptor, ErbB-2 - metabolism</subject><subject>Simian virus 40 large T antigen</subject><subject>Tumor Cells, Cultured</subject><issn>0014-5793</issn><issn>1873-3468</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2002</creationdate><recordtype>article</recordtype><recordid>eNqNUc1u1DAQthCIbhceAeQTag-hduzE8QnRassiVSDRBe3NcuxJMUrsxfaC-gS8Nt4f0SM9WNbMfD-jbxB6RclbSmh7cUsI5VUjJDsj9JywWohq_QTNaCdYxXjbPUWzf5ATdJrSD1Lqjsrn6ITSrqaEixn6s_oO-FOVIU7O6xHbMGnncRjw7TdO8KjjHeAV1j67O_A4wiZCSpBwLrzl4kt94WFbTWCdzmBxjtqnIcRJZxd8oVk8QdYpl9rgTchQhIpNsegjlD422huI6QV6NugxwcvjP0dfrxerq2V18_nDx6v3N5XhdbuuWG8HajsxQMutLE93ne6Z1KYBKtlggTPGeWtkA8xQUWsDgnRSNoLJdujZHL056G5i-LmFlNXkkoFx1B7CNilBecNlyXCOmgPQxJBShEFtopt0vFeUqN0F1P4CahevIlTtL6DWhff6aLDtSywPrGPkBbA8AH67Ee4fp6quF5f1frIbELpv77zeHaSgJPbLQVTJOCh5WhfBZGWD-8-2fwHST6t5</recordid><startdate>20020130</startdate><enddate>20020130</enddate><creator>Chuang, Tzu-Chao</creator><creator>Yu, Yuh-Hua</creator><creator>Lin, Yen-Shing</creator><creator>Wang, Shan-Shue</creator><creator>Kao, Ming-Ching</creator><general>Elsevier B.V</general><scope>6I.</scope><scope>AAFTH</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope></search><sort><creationdate>20020130</creationdate><title>The N-terminal domain of SV40 large T antigen represses the HER2/neu-mediated transformation and metastatic potential in breast cancers</title><author>Chuang, Tzu-Chao ; Yu, Yuh-Hua ; Lin, Yen-Shing ; Wang, Shan-Shue ; Kao, Ming-Ching</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c426X-3bdf1d87fe64d964da88ab39ac5e193fde433446c95e3c172ace7089957396fb3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2002</creationdate><topic>Antigens, Polyomavirus Transforming - chemistry</topic><topic>Antigens, Polyomavirus Transforming - genetics</topic><topic>Antigens, Polyomavirus Transforming - metabolism</topic><topic>Blotting, Western</topic><topic>Breast Neoplasms - genetics</topic><topic>Breast Neoplasms - metabolism</topic><topic>Breast Neoplasms - pathology</topic><topic>Cell Division</topic><topic>Cell Transformation, Neoplastic - genetics</topic><topic>Cell Transformation, Neoplastic - metabolism</topic><topic>Cell Transformation, Neoplastic - pathology</topic><topic>Chemotaxis</topic><topic>Down-Regulation</topic><topic>Female</topic><topic>Gene Expression Regulation, Neoplastic</topic><topic>Genes, erbB-2 - genetics</topic><topic>HER2/neu</topic><topic>Humans</topic><topic>Metastasis</topic><topic>Neoplasm Metastasis - genetics</topic><topic>Neoplasm Metastasis - pathology</topic><topic>p185</topic><topic>Protein Structure, Tertiary</topic><topic>Receptor, ErbB-2 - antagonists & inhibitors</topic><topic>Receptor, ErbB-2 - genetics</topic><topic>Receptor, ErbB-2 - metabolism</topic><topic>Simian virus 40 large T antigen</topic><topic>Tumor Cells, Cultured</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Chuang, Tzu-Chao</creatorcontrib><creatorcontrib>Yu, Yuh-Hua</creatorcontrib><creatorcontrib>Lin, Yen-Shing</creatorcontrib><creatorcontrib>Wang, Shan-Shue</creatorcontrib><creatorcontrib>Kao, Ming-Ching</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>FEBS letters</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Chuang, Tzu-Chao</au><au>Yu, Yuh-Hua</au><au>Lin, Yen-Shing</au><au>Wang, Shan-Shue</au><au>Kao, Ming-Ching</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The N-terminal domain of SV40 large T antigen represses the HER2/neu-mediated transformation and metastatic potential in breast cancers</atitle><jtitle>FEBS letters</jtitle><addtitle>FEBS Lett</addtitle><date>2002-01-30</date><risdate>2002</risdate><volume>511</volume><issue>1</issue><spage>46</spage><epage>50</epage><pages>46-50</pages><issn>0014-5793</issn><eissn>1873-3468</eissn><abstract>HER2/neu is known to be overexpressed in approximately 40% of human breast and ovarian cancers and it is associated with increased metastasis and poor prognosis. We have shown previously that the N-terminal domain of simian virus 40 large T antigen (LT425) can act as a transforming suppressor of the
HER2/
neu oncogene in human ovarian cancer. In the present study, we demonstrate that LT425 can also repress the transforming properties of HER2/neu-overexpressing human breast cancer cells. In addition, the results of a chemotaxis assay and an in vitro chemoinvasion assay further suggest that LT425 can also suppress the metastatic potential of the HER2/neu-transformed breast cancer cells. Taken together, these data clearly suggest that the inhibition of the expression of p185
HER2/neu tyrosine kinase by LT425 is capable of suppressing the HER2/neu-mediated transformation and metastatic potential in breast cancers.</abstract><cop>England</cop><pub>Elsevier B.V</pub><pmid>11821047</pmid><doi>10.1016/S0014-5793(01)03277-X</doi><tpages>5</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | Antigens, Polyomavirus Transforming - chemistry Antigens, Polyomavirus Transforming - genetics Antigens, Polyomavirus Transforming - metabolism Blotting, Western Breast Neoplasms - genetics Breast Neoplasms - metabolism Breast Neoplasms - pathology Cell Division Cell Transformation, Neoplastic - genetics Cell Transformation, Neoplastic - metabolism Cell Transformation, Neoplastic - pathology Chemotaxis Down-Regulation Female Gene Expression Regulation, Neoplastic Genes, erbB-2 - genetics HER2/neu Humans Metastasis Neoplasm Metastasis - genetics Neoplasm Metastasis - pathology p185 Protein Structure, Tertiary Receptor, ErbB-2 - antagonists & inhibitors Receptor, ErbB-2 - genetics Receptor, ErbB-2 - metabolism Simian virus 40 large T antigen Tumor Cells, Cultured |
| title | The N-terminal domain of SV40 large T antigen represses the HER2/neu-mediated transformation and metastatic potential in breast cancers |
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